FUS_PI1HC
ID FUS_PI1HC Reviewed; 555 AA.
AC P12605;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Fusion glycoprotein F0;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1;
DE Flags: Precursor;
GN Name=F;
OS Human parainfluenza 1 virus (strain C39) (HPIV-1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11210;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2847427; DOI=10.1016/0042-6822(88)90058-x;
RA Merson J.R., Hull R.A., Estes M.K., Kasel J.A.;
RT "Molecular cloning and sequence determination of the fusion protein gene of
RT human parainfluenza virus type 1.";
RL Virology 167:97-105(1988).
CC -!- FUNCTION: Class I viral fusion protein. Under the current model, the
CC protein has at least 3 conformational states: pre-fusion native state,
CC pre-hairpin intermediate state, and post-fusion hairpin state. During
CC viral and plasma cell membrane fusion, the heptad repeat (HR) regions
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and plasma cell membranes. Directs fusion of viral and
CC cellular membranes leading to delivery of the nucleocapsid into the
CC cytoplasm. This fusion is pH independent and occurs directly at the
CC outer cell membrane. The trimer of F1-F2 (F protein) probably interacts
CC with HN at the virion surface. Upon HN binding to its cellular
CC receptor, the hydrophobic fusion peptide is unmasked and interacts with
CC the cellular membrane, inducing the fusion between cell and virion
CC membranes. Later in infection, F proteins expressed at the plasma
CC membrane of infected cells could mediate fusion with adjacent cells to
CC form syncytia, a cytopathic effect that could lead to tissue necrosis
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer of disulfide-linked F1-F2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- PTM: The inactive precursor F0 is glycosylated and proteolytically
CC cleaved into F1 and F2 to be functionally active. The cleavage is
CC mediated by cellular proteases during the transport and maturation of
CC the polypeptide (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; M22347; AAA46800.1; -; mRNA.
DR PIR; A31287; VGNZ11.
DR SMR; P12605; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000776; Fusion_F0_Paramyxovir.
DR Pfam; PF00523; Fusion_gly; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..555
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039330"
FT CHAIN 22..112
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039331"
FT CHAIN 113..555
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039332"
FT TOPO_DOM 22..496
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 518..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 113..137
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 138..166
FT /evidence="ECO:0000255"
FT COILED 462..487
FT /evidence="ECO:0000255"
FT SITE 112..113
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 66..195
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250"
FT DISULFID 334..343
FT /evidence="ECO:0000250"
FT DISULFID 358..366
FT /evidence="ECO:0000250"
FT DISULFID 390..395
FT /evidence="ECO:0000250"
FT DISULFID 397..420
FT /evidence="ECO:0000250"
SQ SEQUENCE 555 AA; 60786 MW; 6F0DF6E2C969B9F0 CRC64;
MQKSEILFLI YSSLLLSSSL CQIPVDKLSN VGVIINEGKL LKIAGSYESR YIVLSLVPSI
DLEDGCGTTQ IIQYKNLLNR LLIPLKDALD LQESLITITN DTTVTNDNPQ SRFFGAVIGT
IALGVATAAQ ITAGIALAEA REARKDIALI KDSIIKTHNS VELIQRGIGE QIIALKTLQD
FVNNEIRPAI GELRCETTAL KLGIKLTQHY SELATAFSSN LGTIGEKSLT LQALSSLYSA
NITEILSTIK KDKSDIYDII YTEQVKGTVI DVDLEKYMVT LLVKIPILSE IPGVLIYRAS
SISYNIEGEE WHVAIPNYII NKASSLGGAD VTNCIESRLA YICPRDPTQL IPDNQQKCIL
GDVSKCPVTK VINNLVPKFA FINGGVVANC IASTCTCGTN RIPVNQDRSR GVTFLTYTNC
GLIGINGIEL YANKRGRDTT WGNQIIKVGP AVSIRPVDIS LNLASATNFL EESKIELMKA
KAIISAVGGW HNTESTQIII IIIVCILIII ICGILYYLYR VRRLLVMINS THNSPVNTYT
LESRMRNPYI GNNSN
